3L6G
Crystal structure of lactococcal OpuAC in its open conformation
Summary for 3L6G
| Entry DOI | 10.2210/pdb3l6g/pdb |
| Related | 3l6h |
| Descriptor | Betaine ABC transporter permease and substrate binding protein, 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| Functional Keywords | glycine betaine binding, substrate binding domain, venus fly-trap, cell membrane, membrane, transmembrane, transport, glycine betaine-binding protein |
| Biological source | Lactococcus lactis (Streptococcus lactis) |
| Cellular location | Membrane; Multi-pass membrane protein (By similarity): Q7DAU8 |
| Total number of polymer chains | 1 |
| Total formula weight | 28829.74 |
| Authors | Berntsson, R.P.A.,Wolters, J.C.,Gul, N.,Karasawa, A.,Thunnissen, A.M.W.H.,Slotboom, D.J.,Poolman, B. (deposition date: 2009-12-23, release date: 2010-05-19, Last modification date: 2023-09-06) |
| Primary citation | Wolters, J.C.,Berntsson, R.P.,Gul, N.,Karasawa, A.,Thunnissen, A.M.,Slotboom, D.J.,Poolman, B. Ligand binding and crystal structures of the substrate-binding domain of the ABC transporter OpuA. Plos One, 5:e10361-e10361, 2010 Cited by PubMed Abstract: The ABC transporter OpuA from Lactococcus lactis transports glycine betaine upon activation by threshold values of ionic strength. In this study, the ligand binding characteristics of purified OpuA in a detergent-solubilized state and of its substrate-binding domain produced as soluble protein (OpuAC) was characterized. PubMed: 20454456DOI: 10.1371/journal.pone.0010361 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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